Binding behaviour of a 12-mer peptide and its tandem dimer to gymnospermae and angiospermae lignins

Abstract

The binding behaviour of a 12-mer peptide and its tandem dimer to gymnospermae, Cryptomeria japonica and angiospermae, Eucalyptus globulus lignins was analysed. The tandem dimer significantly changed its conformation upon addition of the lignins to have a 10-times higher affinity than the 12-mer peptide. This result exhibits potential for use as a molecular tool in lignin-degrading (bio)catalysts.